ID Q19579_CAEEL Unreviewed; 692 AA.
AC Q19579;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=Polyadenylate-binding protein {ECO:0000256|RuleBase:RU362004};
DE Short=PABP {ECO:0000256|RuleBase:RU362004};
GN Name=pab-2 {ECO:0000313|EMBL:CAA90444.1,
GN ECO:0000313|WormBase:F18H3.3a};
GN ORFNames=CELE_F18H3.3 {ECO:0000313|EMBL:CAA90444.1}, F18H3.3
GN {ECO:0000313|WormBase:F18H3.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA90444.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA90444.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA90444.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA.
CC {ECO:0000256|RuleBase:RU362004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000256|ARBA:ARBA00008557, ECO:0000256|RuleBase:RU362004}.
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DR EMBL; BX284606; CAA90444.1; -; Genomic_DNA.
DR PIR; T21095; T21095.
DR RefSeq; NP_510260.1; NM_077859.5.
DR AlphaFoldDB; Q19579; -.
DR SMR; Q19579; -.
DR STRING; 6239.F18H3.3a.1; -.
DR EPD; Q19579; -.
DR PaxDb; 6239-F18H3-3a-1; -.
DR PeptideAtlas; Q19579; -.
DR EnsemblMetazoa; F18H3.3a.1; F18H3.3a.1; WBGene00003903.
DR EnsemblMetazoa; F18H3.3a.2; F18H3.3a.2; WBGene00003903.
DR EnsemblMetazoa; F18H3.3a.3; F18H3.3a.3; WBGene00003903.
DR UCSC; F18H3.3a.3; c. elegans.
DR AGR; WB:WBGene00003903; -.
DR WormBase; F18H3.3a; CE02193; WBGene00003903; pab-2.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q19579; -.
DR OMA; NATYSMA; -.
DR OrthoDB; 21912at2759; -.
DR PhylomeDB; Q19579; -.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-72649; Translation initiation complex formation.
DR Reactome; R-CEL-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-CEL-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003903; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; Q19579; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR CDD; cd12378; RRM1_I_PABPs; 1.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR CDD; cd12381; RRM4_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR034364; PABP_RRM1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR NCBIfam; TIGR01628; PABP-1234; 1.
DR PANTHER; PTHR24012:SF712; POLYADENYLATE-BINDING PROTEIN; 1.
DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|RuleBase:RU362004};
KW Proteomics identification {ECO:0007829|EPD:Q19579,
KW ECO:0007829|PeptideAtlas:Q19579};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU362004}.
FT DOMAIN 57..135
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 145..222
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 238..317
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 343..420
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 601..680
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT REGION 507..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 75982 MW; D86D7391304AE773 CRC64;
MAQVPPPMTQ VVTSAPPPTA AATVVAGAVA GQPQAVIQQG PPPTNIGYPP NATYSMASLY
IGDLHPDVSE AMLFEKFSMA GPVLSIRVCR DNTSRLSLGY AYVNFQQPAD AERALDTMNF
EVIHGRPMRI MWSQRDPAAR RAGNGNIFIK NLDRVIDNKS VYDTFSLFGN ILSCKVATDD
EGNSKGYGFV HFETEHSAQT AIEKVNGMLL SDKKVYVGKF QPRAQRMKEL GESGLKYTNV
FVKNFGEHLD QEKLSAMFSK FGEITSAVVM TDAQGKPKGF GFVAFADQDA AGQAVEKLND
SILEGTDCKL SVCRAQKKSE RSAELKRKYE ALKQERVQRY QGVNLYVKNI EEDLNDDGLR
DHFSSFGTIT SAKVMVDENG RSKGFGFVCF EKPEEATAAV TDMNSKMIGA KPLYVALAQR
KEDRRAQLAS QYMQRLATLR MGQQASGVPA MTQLYQPGQQ GYFVPNPMNA QGRPGFQPQS
AQIRGPPGQR VFQNQMFMQY PFNQRQVYPQ QQGRPPMRTN DGRPQYGMAP RPAGAPRVGG
PGVQMGGAPI RQQGPAPRGA PQKPFYQGPP RQQQPQQHSQ QPAQQPGQQG QGQSGIVIHG
QETLTSHMLA QAAPQEQKQL LGERIYALIE KMFPNHKEAG KITGMMLEID NAELIMMLQD
AELFRSKVEE AFGVLTNAQS AAASTSAPTA KN
//
